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Volumn 48, Issue 51, 2009, Pages 12305-12313

Mechanistic studies of para-substituted N,N′-dibenzyl-1,4- diaminobutanes as substrates for a mammalian polyamine oxidase

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDATION; C-H BOND; CHARGED SUBSTRATES; DEUTERIUM KINETIC ISOTOPE EFFECT; DIAMINOBUTANE; DIRECT TRANSFER; GAIN INSIGHT; KINETICS OF OXIDATION; MECHANISTIC STUDIES; MONOAMINE OXIDASE; NEUTRAL NITROGEN; POLYAMINE OXIDASE; RATE LIMITING; VAN DER WAALS VOLUME;

EID: 73149102982     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901694s     Document Type: Article
Times cited : (14)

References (55)
  • 1
    • 34248228763 scopus 로고    scopus 로고
    • Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases
    • Casero, R. A., Jr., and Marton, L. J. (2007) Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases. Nat. Rev. Drug Discovery 6, 373-390.
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 373-390
    • Casero Jr., R.A.1    Marton, L.J.2
  • 2
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • Marton, L. J., and Pegg, A. E. (1995) Polyamines as targets for therapeutic intervention. Annu. Rev. Pharmacol. Toxicol. 35, 55-91.
    • (1995) Annu. Rev. Pharmacol. Toxicol , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 3
    • 32944467076 scopus 로고    scopus 로고
    • Mammalian polyamine catabolism: A therapeutic target, a pathological problem, or both?
    • Wang, Y., and Casero, R. A., Jr. (2006) Mammalian polyamine catabolism: a therapeutic target, a pathological problem, or both? J. Biochem. (Tokyo) 139, 17-25.
    • (2006) J. Biochem. (Tokyo) , vol.139 , pp. 17-25
    • Wang, Y.1    Casero Jr., R.A.2
  • 4
    • 47549106852 scopus 로고    scopus 로고
    • Spermidine/spermine-N1-acetyltransferase: A key metabolic regulator
    • Pegg, A. E. (2008) Spermidine/spermine-N1-acetyltransferase: a key metabolic regulator. Am. J. Physiol. Endocrinol. Metab. 294,E995-E1010.
    • (2008) Am. J. Physiol. Endocrinol. Metab , vol.294
    • Pegg, A.E.1
  • 5
    • 0038419788 scopus 로고    scopus 로고
    • Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase
    • Wu, T., Yankovskaya, V., and McIntire, W. S. (2003) Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase. J. Biol. Chem. 278,20514-20525.
    • (2003) J. Biol. Chem , vol.278 , pp. 20514-20525
    • Wu, T.1    Yankovskaya, V.2    McIntire, W.S.3
  • 6
    • 0029610668 scopus 로고
    • Polyamine oxidase, properties and functions
    • Seiler, N., Peter, M., Yu, K. F. T., and Alan, A. B. (1995) Polyamine oxidase, properties and functions. Prog. Brain Res. 106,333-344.
    • (1995) Prog. Brain Res , vol.106 , pp. 333-344
    • Seiler, N.1    Peter, M.2    Yu, K.F.T.3    Alan, A.B.4
  • 7
    • 0035878846 scopus 로고    scopus 로고
    • Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure
    • Wang, Y., Devereux, W., Woster, P. M., Stewart, T. M., Hacker, A., and Casero, R. A., Jr. (2001) Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure. Cancer Res. 61, 5370-5373.
    • (2001) Cancer Res , vol.61 , pp. 5370-5373
    • Wang, Y.1    Devereux, W.2    Woster, P.M.3    Stewart, T.M.4    Hacker, A.5    Casero Jr., R.A.6
  • 8
    • 0036846756 scopus 로고    scopus 로고
    • Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin
    • Vujcic, S., Diegelman, P., Bacchi, C. J., Kramer, D. L., and Porter, C. W. (2002) Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin. Biochem. J. 367,665-675.
    • (2002) Biochem. J , vol.367 , pp. 665-675
    • Vujcic, S.1    Diegelman, P.2    Bacchi, C.J.3    Kramer, D.L.4    Porter, C.W.5
  • 9
    • 0036140732 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
    • Binda, C., Newton-Vinson, P., Hubalek, F., Edmondson, D. E., and Mattevi, A. (2002) Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat. Struct. Biol. 9,22-26.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 22-26
    • Binda, C.1    Newton-Vinson, P.2    Hubalek, F.3    Edmondson, D.E.4    Mattevi, A.5
  • 11
    • 0034663814 scopus 로고    scopus 로고
    • The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site
    • Pawelek, P. D., Cheah, J., Coulombe, R., Macheroux, P., Ghisla, S., and Vrielink, A. (2000) The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. EMBO J. 19, 4204-4215.
    • (2000) EMBO J , vol.19 , pp. 4204-4215
    • Pawelek, P.D.1    Cheah, J.2    Coulombe, R.3    Macheroux, P.4    Ghisla, S.5    Vrielink, A.6
  • 12
    • 0037025299 scopus 로고    scopus 로고
    • Structurefunction relationships in flavoenzyme dependent amine oxidations. A comparison of polyamine oxidase and monoamine oxidase
    • Binda, C., Mattevi, A., and Edmondson, D. E. (2002) Structurefunction relationships in flavoenzyme dependent amine oxidations. A comparison of polyamine oxidase and monoamine oxidase. J. Biol. Chem. 277, 23973-23976.
    • (2002) J. Biol. Chem , vol.277 , pp. 23973-23976
    • Binda, C.1    Mattevi, A.2    Edmondson, D.E.3
  • 13
    • 0035808250 scopus 로고    scopus 로고
    • FAD-containing polyamine oxidases: A timely challenge for researchers in biochemistry and physiology of plants
    • Sebela, M., Radová, A., Angelini, R., Tavladoraki, P., Frébort, I., and Pec, P. (2001) FAD-containing polyamine oxidases: a timely challenge for researchers in biochemistry and physiology of plants. Plant Sci. 160, 197-207.
    • (2001) Plant Sci , vol.160 , pp. 197-207
    • Sebela, M.1    Radová, A.2    Angelini, R.3    Tavladoraki, P.4    Frébort, I.5    Pec, P.6
  • 14
    • 0037432631 scopus 로고    scopus 로고
    • Yeast Fms1 is a FAD-utilizing polyamine oxidase
    • Landry, J., and Sternglanz, R. (2003) Yeast Fms1 is a FAD-utilizing polyamine oxidase. Biochem. Biophys. Res. Commun. 303, 771-776.
    • (2003) Biochem. Biophys. Res. Commun , vol.303 , pp. 771-776
    • Landry, J.1    Sternglanz, R.2
  • 16
    • 72049099611 scopus 로고    scopus 로고
    • Fitzpatrick, P. F. (2010) Oxidation of amines by flavoproteins, Arch. Biochem. Biophys. (in press).
    • Fitzpatrick, P. F. (2010) Oxidation of amines by flavoproteins, Arch. Biochem. Biophys. (in press).
  • 17
    • 0028877810 scopus 로고
    • Mechanistic probes of monoamine oxidase B catalysis: Rapid-scan stopped flow and magnetic field independence of the reductive half-reaction
    • Miller, J. R., Edmondson, D. E., and Grissom, C. B. (1995) Mechanistic probes of monoamine oxidase B catalysis: rapid-scan stopped flow and magnetic field independence of the reductive half-reaction. J. Am. Chem. Soc. 117, 7830-7831.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 7830-7831
    • Miller, J.R.1    Edmondson, D.E.2    Grissom, C.B.3
  • 18
    • 33845925842 scopus 로고    scopus 로고
    • Mechanistic studies of the flavoenzyme tryptophan 2-monooxygenase: Deuterium and 15N kinetic isotope effects on alanine oxidation by an L-amino acid oxidase
    • Ralph, E. C., Anderson, M. A., Cleland, W. W., and Fitzpatrick, P. F. (2006) Mechanistic studies of the flavoenzyme tryptophan 2-monooxygenase: deuterium and 15N kinetic isotope effects on alanine oxidation by an L-amino acid oxidase. Biochemistry 45, 15844-15852.
    • (2006) Biochemistry , vol.45 , pp. 15844-15852
    • Ralph, E.C.1    Anderson, M.A.2    Cleland, W.W.3    Fitzpatrick, P.F.4
  • 19
    • 34250852848 scopus 로고    scopus 로고
    • Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase
    • Ralph, E. C., Hirschi, J. S., Anderson, M. A., Cleland, W. W., Singleton, D. A., and Fitzpatrick, P. F. (2007) Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase. Biochemistry 46, 7655-7664.
    • (2007) Biochemistry , vol.46 , pp. 7655-7664
    • Ralph, E.C.1    Hirschi, J.S.2    Anderson, M.A.3    Cleland, W.W.4    Singleton, D.A.5    Fitzpatrick, P.F.6
  • 20
    • 18244400100 scopus 로고    scopus 로고
    • Mechanistic studies of mouse polyamine oxidase with N1,N12-bisethylspermine as a substrate
    • Royo, M., and Fitzpatrick, P. F. (2005) Mechanistic studies of mouse polyamine oxidase with N1,N12-bisethylspermine as a substrate. Biochemistry 44, 7079-7084.
    • (2005) Biochemistry , vol.44 , pp. 7079-7084
    • Royo, M.1    Fitzpatrick, P.F.2
  • 21
    • 0028949129 scopus 로고
    • Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 2. pH and kinetic isotope effects
    • Emanuele, J. J., Jr., and Fitzpatrick, P. F. (1995) Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 2. pH and kinetic isotope effects. Biochemistry 34, 3716-3723.
    • (1995) Biochemistry , vol.34 , pp. 3716-3723
    • Emanuele Jr., J.J.1    Fitzpatrick, P.F.2
  • 22
    • 0001319451 scopus 로고
    • Radical ideas about monoamine oxidase
    • Silverman, R. B. (1995) Radical ideas about monoamine oxidase. Acc. Chem. Res. 28, 335-342.
    • (1995) Acc. Chem. Res , vol.28 , pp. 335-342
    • Silverman, R.B.1
  • 23
    • 34547698945 scopus 로고    scopus 로고
    • Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B
    • Edmondson, D. E., Binda, C., and Mattevi, A. (2007) Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B. Arch. Biochem. Biophys. 464, 269-276.
    • (2007) Arch. Biochem. Biophys , vol.464 , pp. 269-276
    • Edmondson, D.E.1    Binda, C.2    Mattevi, A.3
  • 26
    • 61749094173 scopus 로고    scopus 로고
    • pH dependence of amammalian polyamine oxidase: Insights into substrate specificity and the role of lysine 315
    • Henderson Pozzi, M., Gawandi, V., and Fitzpatrick, P. F. (2009) pH dependence of amammalian polyamine oxidase: insights into substrate specificity and the role of lysine 315. Biochemistry 48, 1508-1516.
    • (2009) Biochemistry , vol.48 , pp. 1508-1516
    • Henderson Pozzi, M.1    Gawandi, V.2    Fitzpatrick, P.F.3
  • 27
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W. (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol. 63, 103-138.
    • (1979) Methods Enzymol , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 28
    • 0017580411 scopus 로고
    • Determination of the rate-limiting steps for malic enzyme by the use of isotope effects and other kinetic studies
    • Schimerlik, M. I., Grimshaw, C. E., and Cleland, W. W. (1977) Determination of the rate-limiting steps for malic enzyme by the use of isotope effects and other kinetic studies. Biochemistry 16, 571-576.
    • (1977) Biochemistry , vol.16 , pp. 571-576
    • Schimerlik, M.I.1    Grimshaw, C.E.2    Cleland, W.W.3
  • 29
    • 36849089004 scopus 로고    scopus 로고
    • Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase
    • Fitzpatrick, P. F., Valley, M. P., Bozinovski, D. M., Shaw, P. G., Héroux, A., and Orville, A. M. (2007) Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase. Biochemistry 46, 13800-13808.
    • (2007) Biochemistry , vol.46 , pp. 13800-13808
    • Fitzpatrick, P.F.1    Valley, M.P.2    Bozinovski, D.M.3    Shaw, P.G.4    Héroux, A.5    Orville, A.M.6
  • 30
    • 0019403885 scopus 로고
    • Acetylderivatives as intermediates in polyamine catabolism
    • Bolkenius, F. N., and Seiler, N. (1981) Acetylderivatives as intermediates in polyamine catabolism. Int. J. Biochem. 13, 287-292.
    • (1981) Int. J. Biochem , vol.13 , pp. 287-292
    • Bolkenius, F.N.1    Seiler, N.2
  • 31
    • 4243664295 scopus 로고
    • A survey of Hammett substituent constants and resonance and field parameters
    • Hansch, C., Leo, A., and Taft, R. W. (1991) A survey of Hammett substituent constants and resonance and field parameters. Chem. Rev. 91, 165-195.
    • (1991) Chem. Rev , vol.91 , pp. 165-195
    • Hansch, C.1    Leo, A.2    Taft, R.W.3
  • 32
    • 33749000228 scopus 로고
    • A new substituent constant, π, derived from partition coefficients
    • Fujita, T., Iwasa, J., and Hansch, C. (1964) A new substituent constant, π, derived from partition coefficients. J. Am. Chem. Soc. 86, 5175-5180.
    • (1964) J. Am. Chem. Soc , vol.86 , pp. 5175-5180
    • Fujita, T.1    Iwasa, J.2    Hansch, C.3
  • 33
    • 20544433165 scopus 로고
    • van der Waals volumes and radii
    • Bondi, A. (1964) van der Waals volumes and radii. J. Phys. Chem. 68,441-451.
    • (1964) J. Phys. Chem , vol.68 , pp. 441-451
    • Bondi, A.1
  • 35
    • 33947300443 scopus 로고
    • Nature of the ortho effect. II. Composition of the Taft steric parameters
    • Charton, M. (1969) Nature of the ortho effect. II. Composition of the Taft steric parameters. J. Am. Chem. Soc. 91, 615-618.
    • (1969) J. Am. Chem. Soc , vol.91 , pp. 615-618
    • Charton, M.1
  • 36
    • 0024314707 scopus 로고
    • New substrates of polyamine oxidase dealkylation of N-alkyl-α,o-diamines
    • Bolkenius, F. N., and Seiler, N. (1989) New substrates of polyamine oxidase dealkylation of N-alkyl-α,o-diamines. Biol. Chem. Hoppe-Seyler 370, 525-531.
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 525-531
    • Bolkenius, F.N.1    Seiler, N.2
  • 37
    • 0019524346 scopus 로고
    • pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same
    • Cook, P. F., and Cleland, W. W. (1981) pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same. Biochemistry 20, 1797-1805.
    • (1981) Biochemistry , vol.20 , pp. 1797-1805
    • Cook, P.F.1    Cleland, W.W.2
  • 38
    • 67049098986 scopus 로고    scopus 로고
    • Use of pH and kinetic isotope effects to establish chemistry as rate-limiting in oxidation of a peptide substrate by LSD1
    • Gaweska, H., Henderson Pozzi, M., Schmidt, D. M. Z., McCafferty, D. G., and Fitzpatrick, P. F. (2009) Use of pH and kinetic isotope effects to establish chemistry as rate-limiting in oxidation of a peptide substrate by LSD1. Biochemistry 48, 5440-5445.
    • (2009) Biochemistry , vol.48 , pp. 5440-5445
    • Gaweska, H.1    Henderson Pozzi, M.2    Schmidt, D.M.Z.3    McCafferty, D.G.4    Fitzpatrick, P.F.5
  • 39
    • 0026767696 scopus 로고
    • pH and kinetic isotope effects on the reductive half-reaction of D-amino acid oxidase
    • Denu, J. M., and Fitzpatrick, P. F. (1992) pH and kinetic isotope effects on the reductive half-reaction of D-amino acid oxidase. Biochemistry 31, 8207-8215.
    • (1992) Biochemistry , vol.31 , pp. 8207-8215
    • Denu, J.M.1    Fitzpatrick, P.F.2
  • 41
    • 33847800931 scopus 로고
    • Ionization constants of substituted 2-aminoacetanilides and benzylamines. Transmission of electronic effects through amide links
    • Peters, F. B., and Johnson, H. W., Jr. (1975) Ionization constants of substituted 2-aminoacetanilides and benzylamines. Transmission of electronic effects through amide links. J. Org. Chem. 40, 1517-1519.
    • (1975) J. Org. Chem , vol.40 , pp. 1517-1519
    • Peters, F.B.1    Johnson Jr., H.W.2
  • 42
    • 0011786864 scopus 로고
    • Prediction of the strengths of organic bases
    • Clark, J., and Perrin, D. D. (1964) Prediction of the strengths of organic bases. Q. Rev. Chem. Soc. 18, 295-320.
    • (1964) Q. Rev. Chem. Soc , vol.18 , pp. 295-320
    • Clark, J.1    Perrin, D.D.2
  • 43
    • 0035814939 scopus 로고    scopus 로고
    • Structural bases for inhibitor binding and catalysis in polyamine oxidase
    • Binda, C., Angelini, R., Federico, R., Ascenzi, P., and Mattevi, A. (2001) Structural bases for inhibitor binding and catalysis in polyamine oxidase. Biochemistry 40, 2766-2776.
    • (2001) Biochemistry , vol.40 , pp. 2766-2776
    • Binda, C.1    Angelini, R.2    Federico, R.3    Ascenzi, P.4    Mattevi, A.5
  • 44
    • 17444422874 scopus 로고    scopus 로고
    • Crystal structures of Fms1 and its complex with spermine reveal substrate specificity
    • Huang, Q., Liu, Q., and Hao, Q. (2005) Crystal structures of Fms1 and its complex with spermine reveal substrate specificity. J. Mol. Biol. 348, 951-959.
    • (2005) J. Mol. Biol , vol.348 , pp. 951-959
    • Huang, Q.1    Liu, Q.2    Hao, Q.3
  • 45
    • 0033550070 scopus 로고    scopus 로고
    • Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A
    • Miller, J. R., and Edmondson, D. E. (1999) Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A. Biochemistry 38,13670-13683.
    • (1999) Biochemistry , vol.38 , pp. 13670-13683
    • Miller, J.R.1    Edmondson, D.E.2
  • 46
    • 1942485882 scopus 로고    scopus 로고
    • Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations
    • Fitzpatrick, P. F. (2004) Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations. Bioorg. Chem. 32,125-139.
    • (2004) Bioorg. Chem , vol.32 , pp. 125-139
    • Fitzpatrick, P.F.1
  • 47
    • 0021799987 scopus 로고
    • 3-Phenylpropenes as mechanism-based inhibitors of dopamine β-hydroxylase: Evidence for a radical mechanism
    • Fitzpatrick, P. F., Flory, D. R., Jr., and Villafranca, J. J. (1985) 3-Phenylpropenes as mechanism-based inhibitors of dopamine β-hydroxylase: evidence for a radical mechanism. Biochemistry 24,2108-2114.
    • (1985) Biochemistry , vol.24 , pp. 2108-2114
    • Fitzpatrick, P.F.1    Flory Jr., D.R.2    Villafranca, J.J.3
  • 48
    • 11144270176 scopus 로고    scopus 로고
    • Chemical aspects of amine oxidation by flavoprotein enzymes
    • Scrutton, N. S. (2004) Chemical aspects of amine oxidation by flavoprotein enzymes. Nat. Prod. Rep. 21, 722-730.
    • (2004) Nat. Prod. Rep , vol.21 , pp. 722-730
    • Scrutton, N.S.1
  • 49
    • 0031054686 scopus 로고    scopus 로고
    • On the mechanism of D-amino acid oxidase. Structure/linear free energy correlations and deuterium kinetic isotope effects using substituted phenylgylcines
    • Pollegioni, L., Blodig, W., and Ghisla, S. (1997) On the mechanism of D-amino acid oxidase. Structure/linear free energy correlations and deuterium kinetic isotope effects using substituted phenylgylcines. J. Biol. Chem. 272, 4924-4934.
    • (1997) J. Biol. Chem , vol.272 , pp. 4924-4934
    • Pollegioni, L.1    Blodig, W.2    Ghisla, S.3
  • 50
    • 0034642217 scopus 로고    scopus 로고
    • Structure-activity relations in the oxidation of phenethylamine analogues by recombinant human liver monoamine oxidase A
    • Nandigama, R. K., and Edmondson, D. E. (2000) Structure-activity relations in the oxidation of phenethylamine analogues by recombinant human liver monoamine oxidase A. Biochemistry 39, 15258-15265.
    • (2000) Biochemistry , vol.39 , pp. 15258-15265
    • Nandigama, R.K.1    Edmondson, D.E.2
  • 52
    • 0028278443 scopus 로고
    • Structure-activity relationships in the oxidation of benzylamine analogues by bovine liver mitochondrial monoamine oxidase B
    • Walker, M. C., and Edmondson, D. E. (1994) Structure-activity relationships in the oxidation of benzylamine analogues by bovine liver mitochondrial monoamine oxidase B. Biochemistry 33, 7088-7098.
    • (1994) Biochemistry , vol.33 , pp. 7088-7098
    • Walker, M.C.1    Edmondson, D.E.2
  • 53
    • 0034722962 scopus 로고    scopus 로고
    • Nitrogen isotope effects as probes of the mechanism of D-amino acid oxidase
    • Kurtz, K. A., Rishavy, M. A., Cleland, W. W., and Fitzpatrick, P. F. (2000) Nitrogen isotope effects as probes of the mechanism of D-amino acid oxidase. J. Am. Chem. Soc. 122, 12896-12897.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 12896-12897
    • Kurtz, K.A.1    Rishavy, M.A.2    Cleland, W.W.3    Fitzpatrick, P.F.4
  • 54
    • 33847013408 scopus 로고    scopus 로고
    • The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation
    • Faust, A., Niefind, K., Hummel, W., and Schomburg, D. (2007) The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation. J. Mol. Biol. 367, 234-248.
    • (2007) J. Mol. Biol , vol.367 , pp. 234-248
    • Faust, A.1    Niefind, K.2    Hummel, W.3    Schomburg, D.4
  • 55
    • 47249152398 scopus 로고    scopus 로고
    • The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzymesubstrate complex
    • Dunn, R. V., Marshall, K. R., Munro, A. W., and Scrutton, N. S. (2008) The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzymesubstrate complex. FEBS J. 275, 3850-3858.
    • (2008) FEBS J , vol.275 , pp. 3850-3858
    • Dunn, R.V.1    Marshall, K.R.2    Munro, A.W.3    Scrutton, N.S.4


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